BAAT_RAT
ID BAAT_RAT Reviewed; 420 AA.
AC Q63276; Q5M8A2;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Bile acid-CoA:amino acid N-acyltransferase;
DE Short=BACAT;
DE Short=BAT;
DE EC=2.3.1.65 {ECO:0000269|PubMed:12951368, ECO:0000269|PubMed:624713};
DE AltName: Full=Bile acid-CoA thioesterase {ECO:0000250|UniProtKB:Q14032};
DE AltName: Full=Choloyl-CoA hydrolase;
DE EC=3.1.2.27 {ECO:0000250|UniProtKB:Q14032};
DE AltName: Full=Glycine N-choloyltransferase;
DE AltName: Full=Kan-1;
DE AltName: Full=Long-chain fatty-acyl-CoA hydrolase;
DE EC=3.1.2.2 {ECO:0000250|UniProtKB:Q14032};
GN Name=Baat;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=7575455; DOI=10.1042/bj3110203;
RA Furutani M., Arii S., Higashitsuji H., Mise M., Fukumoto M., Takano S.,
RA Nakayama H., Imamura M., Fujita J.;
RT "Reduced expression of kan-1 (encoding putative bile acid-CoA-amino acid N-
RT acyltransferase) mRNA in livers of rats after partial hepatectomy and
RT during sepsis.";
RL Biochem. J. 311:203-208(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Liver;
RX PubMed=12951368; DOI=10.1194/jlr.m300128-jlr200;
RA He D., Barnes S., Falany C.N.;
RT "Rat liver bile acid CoA:amino acid N-acyltransferase: expression,
RT characterization, and peroxisomal localization.";
RL J. Lipid Res. 44:2242-2249(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Liver;
RX PubMed=624713; DOI=10.1016/s0021-9258(17)38103-6;
RA Killenberg P.G., Jordan J.T.;
RT "Purification and characterization of bile acid-CoA:amino acid N-
RT acyltransferase from rat liver.";
RL J. Biol. Chem. 253:1005-1010(1978).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-418, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalyzes the amidation of bile acids (BAs) with the amino
CC acids taurine and glycine (PubMed:12951368, PubMed:624713). More
CC efficient at taurine conjugation of cholyl CoA than glycine conjugation
CC (PubMed:12951368, PubMed:624713). Amidation of BAs in the liver with
CC glycine or taurine prior to their excretion into bile is an important
CC biochemical event in bile acid metabolism (By similarity). This
CC conjugation (or amidation) plays several important biological roles in
CC that it promotes the secretion of BAs and cholesterol into bile and
CC increases the detergent properties of BAs in the intestine, which
CC facilitates lipid and vitamin absorption (By similarity). May also act
CC as an acyl-CoA thioesterase that regulates intracellular levels of free
CC fatty acids (By similarity). In vitro, catalyzes the hydrolysis of
CC long- and very long-chain saturated acyl-CoAs to the free fatty acid
CC and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs (By
CC similarity). {ECO:0000250|UniProtKB:Q14032,
CC ECO:0000269|PubMed:12951368, ECO:0000269|PubMed:624713}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choloyl-CoA + glycine = CoA + glycocholate + H(+);
CC Xref=Rhea:RHEA:14001, ChEBI:CHEBI:15378, ChEBI:CHEBI:29746,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:57373; EC=2.3.1.65;
CC Evidence={ECO:0000269|PubMed:12951368, ECO:0000269|PubMed:624713};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14002;
CC Evidence={ECO:0000305|PubMed:12951368, ECO:0000305|PubMed:624713};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choloyl-CoA + H2O = cholate + CoA + H(+);
CC Xref=Rhea:RHEA:14541, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29747, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373; EC=3.1.2.27;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14542;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholoyl-CoA + H2O = chenodeoxycholate + CoA + H(+);
CC Xref=Rhea:RHEA:31511, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:36234, ChEBI:CHEBI:57287, ChEBI:CHEBI:62989; EC=3.1.2.27;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31512;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+);
CC Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate;
CC Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoyl-CoA + H2O = CoA + docosanoate + H(+);
CC Xref=Rhea:RHEA:40783, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:23858, ChEBI:CHEBI:57287, ChEBI:CHEBI:65059;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40784;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetracosanoyl-CoA = CoA + H(+) + tetracosanoate;
CC Xref=Rhea:RHEA:40787, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31014, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40788;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexacosanoyl-CoA = CoA + H(+) + hexacosanoate;
CC Xref=Rhea:RHEA:40791, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31013, ChEBI:CHEBI:57287, ChEBI:CHEBI:64868;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40792;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+);
CC Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choloyl-CoA + taurine = CoA + H(+) + taurocholate;
CC Xref=Rhea:RHEA:47100, ChEBI:CHEBI:15378, ChEBI:CHEBI:36257,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57373, ChEBI:CHEBI:507393;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47101;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholoyl-CoA + glycine = CoA + glycochenodeoxycholate
CC + H(+); Xref=Rhea:RHEA:49788, ChEBI:CHEBI:15378, ChEBI:CHEBI:36252,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:62989;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49789;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholoyl-CoA + taurine = CoA + H(+) +
CC taurochenodeoxycholate; Xref=Rhea:RHEA:49784, ChEBI:CHEBI:9407,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:62989,
CC ChEBI:CHEBI:507393; Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49785;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + glycine = CoA + H(+) + N-eicosanoylglycinate;
CC Xref=Rhea:RHEA:49792, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57380, ChEBI:CHEBI:87391;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49793;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + hexacosanoyl-CoA = CoA + H(+) + N-
CC hexacosanoylglycine; Xref=Rhea:RHEA:49772, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:64868,
CC ChEBI:CHEBI:87414; Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49773;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoyl-CoA + glycine = CoA + H(+) + N-docosanoylglycine;
CC Xref=Rhea:RHEA:49780, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:65059, ChEBI:CHEBI:87410;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49781;
CC Evidence={ECO:0000250|UniProtKB:Q14032};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.0 mM for taurine toward choloyl-CoA
CC {ECO:0000269|PubMed:7575455};
CC KM=4.4 mM for glycine toward choloyl-CoA
CC {ECO:0000269|PubMed:7575455};
CC KM=20 uM for glycine toward choloyl-CoA {ECO:0000269|PubMed:624713};
CC KM=10 uM for taurine toward choloyl-CoA {ECO:0000269|PubMed:624713};
CC KM=15 uM for glycine toward deoxycholoyl-CoA
CC {ECO:0000269|PubMed:624713};
CC KM=13 uM for taurine toward deoxycholoyl-CoA
CC {ECO:0000269|PubMed:624713};
CC KM=13 uM for glycine toward chenodeoxycholoyl-CoA
CC {ECO:0000269|PubMed:624713};
CC KM=16 uM for taurine toward chenodeoxycholoyl-CoA
CC {ECO:0000269|PubMed:624713};
CC KM=12 uM for glycine toward lithocholoyl-CoA
CC {ECO:0000269|PubMed:624713};
CC KM=11 uM for taurine toward lithocholoyl-CoA
CC {ECO:0000269|PubMed:624713};
CC Vmax=8.69 umol/min/mg enzyme for glycine toward choloyl-CoA
CC {ECO:0000269|PubMed:624713};
CC Vmax=4.09 umol/min/mg enzyme for taurine toward choloyl-CoA
CC {ECO:0000269|PubMed:624713};
CC Vmax=7.34 umol/min/mg enzyme for glycine toward deoxycholoyl-CoA
CC {ECO:0000269|PubMed:624713};
CC Vmax=3.10 umol/min/mg enzyme for taurine toward deoxycholoyl-CoA
CC {ECO:0000269|PubMed:624713};
CC Vmax=5.20 umol/min/mg enzyme for glycine toward chenodeoxycholoyl-CoA
CC {ECO:0000269|PubMed:624713};
CC Vmax=3.05 umol/min/mg enzyme for taurine toward chenodeoxycholoyl-CoA
CC {ECO:0000269|PubMed:624713};
CC Vmax=5.26 umol/min/mg enzyme for glycine toward lithocholoyl-CoA
CC {ECO:0000269|PubMed:624713};
CC Vmax=3.42 umol/min/mg enzyme for taurine toward lithocholoyl-CoA
CC {ECO:0000269|PubMed:624713};
CC pH dependence:
CC Optimum pH is 7.8. {ECO:0000269|PubMed:624713};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q14032}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:12951368}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:12951368}.
CC -!- TISSUE SPECIFICITY: Expressed in liver (at protein level); found in
CC hepatocytes, sinusoidal endothelial cells and Kupffer cells.
CC {ECO:0000269|PubMed:12951368, ECO:0000269|PubMed:7575455}.
CC -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC {ECO:0000305}.
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DR EMBL; D43964; BAA07901.1; -; mRNA.
DR EMBL; BC088153; AAH88153.1; -; mRNA.
DR PIR; S59131; S59131.
DR RefSeq; NP_058996.2; NM_017300.2.
DR AlphaFoldDB; Q63276; -.
DR SMR; Q63276; -.
DR STRING; 10116.ENSRNOP00000009777; -.
DR ESTHER; ratno-BAAT; Acyl-CoA_Thioesterase.
DR MEROPS; S09.A50; -.
DR CarbonylDB; Q63276; -.
DR iPTMnet; Q63276; -.
DR PhosphoSitePlus; Q63276; -.
DR PaxDb; Q63276; -.
DR PRIDE; Q63276; -.
DR Ensembl; ENSRNOT00000009777; ENSRNOP00000009777; ENSRNOG00000007395.
DR GeneID; 29725; -.
DR KEGG; rno:29725; -.
DR UCSC; RGD:2190; rat.
DR CTD; 570; -.
DR RGD; 2190; Baat.
DR eggNOG; ENOG502QQ8Z; Eukaryota.
DR GeneTree; ENSGT01010000222336; -.
DR HOGENOM; CLU_029849_4_0_1; -.
DR InParanoid; Q63276; -.
DR OMA; LTPFQVV; -.
DR OrthoDB; 1260385at2759; -.
DR PhylomeDB; Q63276; -.
DR TreeFam; TF314911; -.
DR BioCyc; MetaCyc:MON-14337; -.
DR Reactome; R-RNO-159418; Recycling of bile acids and salts.
DR Reactome; R-RNO-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR SABIO-RK; Q63276; -.
DR PRO; PR:Q63276; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007395; Expressed in liver and 15 other tissues.
DR Genevisible; Q63276; RN.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0033882; F:choloyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0047963; F:glycine N-choloyltransferase activity; IDA:UniProtKB.
DR GO; GO:0052816; F:long-chain acyl-CoA hydrolase activity; ISO:RGD.
DR GO; GO:0052815; F:medium-chain acyl-CoA hydrolase activity; ISO:RGD.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016410; F:N-acyltransferase activity; ISO:RGD.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0052817; F:very long chain acyl-CoA hydrolase activity; ISO:RGD.
DR GO; GO:0006637; P:acyl-CoA metabolic process; ISO:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0006699; P:bile acid biosynthetic process; ISO:RGD.
DR GO; GO:0002152; P:bile acid conjugation; IDA:UniProtKB.
DR GO; GO:0008206; P:bile acid metabolic process; ISO:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0006544; P:glycine metabolic process; ISO:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0019530; P:taurine metabolic process; ISO:RGD.
DR Gene3D; 2.60.40.2240; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR016662; Acyl-CoA_thioEstase_long-chain.
DR InterPro; IPR014940; BAAT_C.
DR InterPro; IPR006862; Thio_Ohase/aa_AcTrfase.
DR InterPro; IPR042490; Thio_Ohase/BAAT_N.
DR Pfam; PF08840; BAAT_C; 1.
DR Pfam; PF04775; Bile_Hydr_Trans; 1.
DR PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Fatty acid metabolism; Hydrolase;
KW Lipid metabolism; Peroxisome; Phosphoprotein; Reference proteome;
KW Serine esterase; Transferase.
FT CHAIN 1..420
FT /note="Bile acid-CoA:amino acid N-acyltransferase"
FT /id="PRO_0000202161"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 328
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 362
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 40
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91X34"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 346
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91X34"
FT MOD_RES 350
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91X34"
FT MOD_RES 409
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91X34"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 133
FT /note="V -> M (in Ref. 1; BAA07901)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 46465 MW; AACDB03726EB546F CRC64;
MAKLTAVPLS ALVDEPVHIR VTGLTPFQVV CLQASLKDDK GNLFNSQAFY RASEVGEVDL
ERDSSLGGDY MGVHPMGLFW SMKPEKLLTR LVKRDVMNRP HKVHIKLCHP YFPVEGKVIS
SSLDSLILER WYVAPGVTRI HVKEGRIRGA LFLPPGEGPF PGVIDLFGGA GGLFEFRASL
LASHGFATLA LAYWGYDDLP SRLEKVDLEY FEEGVEFLLR HPKVLGPGVG ILSVCIGAEI
GLSMAINLKQ ITATVLINGP NFVSSNPHVY RGKVFQPTPC SEEFVTTNAL GLVEFYRTFE
ETADKDSKYC FPIEKAHGHF LFVVGEDDKN LNSKVHAKQA IAQLMKSGKK NWTLLSYPGA
GHLIEPPYSP LCSASRMPFV IPSINWGGEV IPHAAAQEHS WKEIQKFLKQ HLNPGFNSQL
